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On the interactions of the receptor-binding domain of SARS-CoV-1 and SARS-CoV-2 spike proteins with monoclonal antibodies and the receptor ACE2.
Corrêa Giron, Carolina; Laaksonen, Aatto; Barroso da Silva, Fernando L.
Afiliação
  • Corrêa Giron C; Universidade Federal do Triângulo Mineiro, Departamento de Saúde Coletiva, Rua Vigário Carlos, 38025-350 Uberaba, MG, Brazil; Universidade de São Paulo, Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Av. café, s/no - campus da USP, BR-14040-903 Ribeirão Preto SP, Brazil.
  • Laaksonen A; Department of Materials and Environmental Chemistry, Arrhenius Laboratory, Stockholm University, SE-106 91 Stockholm, Sweden; State Key Laboratory of Materials-Oriented and Chemical Engineering, Nanjing Tech University, Nanjing, 210009, PR China; Centre of Advanced Research in Bionanoconjugates and Biopolymers, Petru Poni Institute of Macromolecular Chemistry, Aleea Grigore Ghica-Voda, 41A, 700487 Iasi, Romania; Department of Engineering Sciences and Mathematics, Division of Energy Science, Lule
  • Barroso da Silva FL; Universidade de São Paulo, Departamento de Ciências Biomoleculares, Faculdade de Ciências Farmacêuticas de Ribeirão Preto, Av. café, s/no - campus da USP, BR-14040-903 Ribeirão Preto SP, Brazil; Department of Chemical and Biomolecular Engineering, North Carolina State University, Raleigh, NC 27695, United States. Electronic address: flbarroso@usp.br.
Virus Res ; 285: 198021, 2020 08.
Article em En | MEDLINE | ID: mdl-32416259
A new betacoronavirus named SARS-CoV-2 has emerged as a new threat to global health and economy. A promising target for both diagnosis and therapeutics treatments of the new disease named COVID-19 is the coronavirus (CoV) spike (S) glycoprotein. By constant-pH Monte Carlo simulations and the PROCEEDpKa method, we have mapped the electrostatic epitopes for four monoclonal antibodies and the angiotensin-converting enzyme 2 (ACE2) on both SARS-CoV-1 and the new SARS-CoV-2 S receptor binding domain (RBD) proteins. We also calculated free energy of interactions and shown that the S RBD proteins from both SARS viruses binds to ACE2 with similar affinities. However, the affinity between the S RBD protein from the new SARS-CoV-2 and ACE2 is higher than for any studied antibody previously found complexed with SARS-CoV-1. Based on physical chemical analysis and free energies estimates, we can shed some light on the involved molecular recognition processes, their clinical aspects, the implications for drug developments, and suggest structural modifications on the CR3022 antibody that would improve its binding affinities for SARS-CoV-2 and contribute to address the ongoing international health crisis.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptores Virais / Peptidil Dipeptidase A / Coronavírus Relacionado à Síndrome Respiratória Aguda Grave / Glicoproteína da Espícula de Coronavírus / Betacoronavirus Limite: Humans Idioma: En Revista: Virus Res Assunto da revista: VIROLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Receptores Virais / Peptidil Dipeptidase A / Coronavírus Relacionado à Síndrome Respiratória Aguda Grave / Glicoproteína da Espícula de Coronavírus / Betacoronavirus Limite: Humans Idioma: En Revista: Virus Res Assunto da revista: VIROLOGIA Ano de publicação: 2020 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda